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Sheng-Huei Yang,Ching-Ming Chien,Mei-Chin Lu,Yi-Hsiung Lin,Xiu-Wei Hu,Shinne-Ren Lin 생화학분자생물학회 2006 Experimental and molecular medicine Vol.38 No.4
Cardiotoxin III (CTX III), a basic polypeptide with 60 amino acid residues isolated from Naja naja atra venom, has been reported to have anticancer activity. CTX III-induced K562 cell apoptosis was confirmed by DNA fragmentation (DNA ladder, sub-G1 for-mation) and phosphatidylserine (PS) externalization with an IC50 value of 1.7 g/ml at 48 h. A mechanistic analysis demonstrated that CTX III-induced apop-totic cell death was accompanied by up-regulation of both Bax and endonuclease G (Endo G), and downregulation of Bcl-XL. CTX III had no effect on the levels of Bcl-2, Bid, XIAP survivin, and AIF proteins. CTX III treatment caused loss of the mitochondrial membrane potential (Ψm), release of mitochon-drial cytochrome c to the cytosol, and activation of both caspase-9 and -3. CTX III-induced apoptosis was significantly blocked by the broad-spectrum cas-pase inhibitor Z-VAD-FMK. However, CTX III did not generate reactive oxygen species (ROS) and talase, did not block CTX III-induced apoptosis in K562 cells. Modulation of Bax, Bcl-XL, and the Endo G proteins, release of mitochondrial cytochome c, and activation of caspase-3 and -9 all are involved in the CTX III-triggered apoptotic process in human leukemia K562 cells.
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